Mutation:BRCA1

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Sequence

mutations with manual annotation;pathogenic;benign;not yet reviewed;
wild typeShow which residues have mutations:
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<StructureSection load='' size='340' side='right' caption='' scene=''>
<StructureSection load='' size='340' side='right' caption='' scene=''>
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'''Some interesting mutation exaamples''':
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'''Some interesting mutation examples''':
* [http://proteopedia.org/w/Mutation:BRCA1?res=39&mut=R Cys39Arg]
* [http://proteopedia.org/w/Mutation:BRCA1?res=39&mut=R Cys39Arg]

Revision as of 10:05, 13 June 2019

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References

  1. Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ. Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer. Nat Struct Mol Biol. 2004 Jun;11(6):512-8. Epub 2004 May 9. PMID:15133502 doi:10.1038/nsmb775
  2. Yue P, Li Z, Moult J. Loss of protein structure stability as a major causative factor in monogenic disease. J Mol Biol. 2005 Oct 21;353(2):459-73. PMID:16169011 doi:http://dx.doi.org/10.1016/j.jmb.2005.08.020

Proteopedia Page Contributors and Editors (what is this?)

Jaime Prilusky, John Moult, Lipika Ray, Joel L. Sussman, Angel Herraez

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